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   <subfield code="a">α- d -Galactosylation of surface fucoglycoconjugate(s) upon stimulation/activation of murine peritoneal macrophages</subfield>
   <subfield code="h">[Elektronische Daten]</subfield>
   <subfield code="c">[Jerzy Petryniak]</subfield>
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   <subfield code="a">Murine resident macrophages express, on their surface, carbohydrate epitopes which undergo changes during their stimulation/activation as monitored by binding of125I labelledEvonymus europaea andGriffonia simplicifolia I-B4 lectins. Treatment of the stimulated macrophages with coffee bean α-galactosidase abolished binding of the GS I-B4 isolectin and changed the binding pattern of theEvonymus lectin. The affinity (K a) ofEvonymus lectin for α-galactosidase-treated macrophages decreased approximately 23-fold, from 1.25×108 M−1 to 5.5×106 M−1. Subsequent digestion of α-galactosidase-treated macrophages with α-l-fucosidase fromTrichomonas foetus, further reduced binding ofEvonymus lectin. Resident macrophages showed the same pattern ofEvonymus lectin binding, with the same affinity, as α-galactosidase-treated, stimulated macrophages. These results, together with a consideration of the carbohydrate binding specificity of theEvonymus lectin which, in the absence of α-d-galactosyl groups, requires α-l-fucosyl groups for binding, indicate the presence, on resident macrophages, of glycoconjugates with terminal α-l-fucosyl residues. It is also concluded that during macrophage stimulation/activation α-d-galactosyl residues are added to this glycoconjugate and that they form part of the receptor forEvonymus lectin. The same glycoconjugate(s) is/are also expressed on the activated macrophage IC-21 cell line which exhibits the same characteristics as that of stimulated peritoneal macrophages, i.e., it contains α-d-galactosyl end groups and is resistant to the action of trypsin. Both lectins were also specifically bound toCorynaebacterium parvum activated macrophages.</subfield>
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   <subfield code="a">Metadata rights reserved</subfield>
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